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Protein

Fibrillin-2

Gene

FBN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Fibrillin-2: Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138829-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1566948. Elastic fibre formation.
R-HSA-2129379. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-2
Cleaved into the following chain:
Gene namesi
Name:FBN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:3604. FBN2.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • microfibril Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Arthrogryposis, distal, 9 (DA9)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of distal arthrogryposis, a disease characterized by congenital joint contractures that mainly involve two or more distal parts of the limbs, in the absence of a primary neurological or muscle disease. DA9 is a connective tissue disorder characterized by contractures, arachnodactyly, scoliosis, and crumpled ears.
See also OMIM:121050
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015851391E → K in DA9. Corresponds to variant rs137852826dbSNPEnsembl.1
Natural variantiVAR_058364754G → S in DA9. 1 PublicationCorresponds to variant rs145259927dbSNPEnsembl.1
Natural variantiVAR_0549811057G → D in DA9. 2 Publications1
Natural variantiVAR_0583651091N → S in DA9. 1 Publication1
Natural variantiVAR_0549821093I → T in DA9. 2 Publications1
Natural variantiVAR_0107391115D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 PublicationsCorresponds to variant rs137852827dbSNPEnsembl.1
Natural variantiVAR_0583661122S → P in DA9. 1 Publication1
Natural variantiVAR_0107401142C → F in DA9. 2 PublicationsCorresponds to variant rs137852828dbSNPEnsembl.1
Natural variantiVAR_0583671142C → R in DA9. 1 Publication1
Natural variantiVAR_0583681146Y → C in DA9. 1 Publication1
Natural variantiVAR_0583691156C → F in DA9. 1 Publication1
Natural variantiVAR_0583701161E → K in DA9. 1 Publication1
Natural variantiVAR_0549831179G → C in DA9. 1 Publication1
Natural variantiVAR_0549841198C → Y in DA9. 1 Publication1
Natural variantiVAR_0549851240C → R in DA9. 1 Publication1
Natural variantiVAR_0583711246C → F in DA9. 1 Publication1
Natural variantiVAR_0107411253C → W in DA9. 2 PublicationsCorresponds to variant rs28931602dbSNPEnsembl.1
Natural variantiVAR_0023501253C → Y in DA9. 2 PublicationsCorresponds to variant rs137852825dbSNPEnsembl.1
Natural variantiVAR_0764821257C → R in DA9. 1 Publication1
Natural variantiVAR_0549861257C → W in DA9. 1 Publication1
Natural variantiVAR_0726531259N → K in DA9. 1 PublicationCorresponds to variant rs267606802dbSNPEnsembl.1
Natural variantiVAR_0549871268C → R in DA9. 1 Publication1
Natural variantiVAR_0583721384C → F in DA9. 1 Publication1
Natural variantiVAR_0583731384C → Y in DA9. 1 PublicationCorresponds to variant rs794727560dbSNPEnsembl.1
Natural variantiVAR_0740521406C → R in DA9. 1 Publication1
Natural variantiVAR_0583741408D → N in DA9. 1 Publication1
Natural variantiVAR_0583751425C → R in DA9. 1 Publication1
Natural variantiVAR_0023511434C → S in DA9. 2 Publications1
Macular degeneration, early-onset (EOMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn ocular disorder characterized by macular changes resulting in progressive loss of visual acuity.
See also OMIM:616118
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0726511144E → K in EOMD. 1 PublicationCorresponds to variant rs200060005dbSNPEnsembl.1
Natural variantiVAR_0726521247M → T in EOMD. 1 PublicationCorresponds to variant rs149054177dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2201.
MalaCardsiFBN2.
MIMi121050. phenotype.
616118. phenotype.
OpenTargetsiENSG00000138829.
Orphaneti279. Age-related macular degeneration.
115. Congenital contractural arachnodactyly.
PharmGKBiPA28017.

Polymorphism and mutation databases

BioMutaiFBN2.
DMDMi238054385.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
PropeptideiPRO_000043688729 – 77CuratedAdd BLAST49
ChainiPRO_000000758478 – 2779Fibrillin-2CuratedAdd BLAST2702
ChainiPRO_00004368882780 – 2912Fibrillin-2 C-terminal peptideBy similarityAdd BLAST133

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi115 ↔ 124PROSITE-ProRule annotation
Disulfide bondi119 ↔ 130PROSITE-ProRule annotation
Disulfide bondi132 ↔ 141PROSITE-ProRule annotation
Disulfide bondi149 ↔ 159PROSITE-ProRule annotation
Disulfide bondi153 ↔ 164PROSITE-ProRule annotation
Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
Disulfide bondi180 ↔ 190PROSITE-ProRule annotation
Disulfide bondi184 ↔ 196PROSITE-ProRule annotation
Disulfide bondi198 ↔ 207PROSITE-ProRule annotation
Disulfide bondi280 ↔ 292PROSITE-ProRule annotation
Disulfide bondi287 ↔ 301PROSITE-ProRule annotation
Disulfide bondi303 ↔ 316PROSITE-ProRule annotation
Disulfide bondi322 ↔ 334PROSITE-ProRule annotation
Disulfide bondi329 ↔ 343PROSITE-ProRule annotation
Disulfide bondi345 ↔ 358PROSITE-ProRule annotation
Glycosylationi492N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi498 ↔ 510PROSITE-ProRule annotation
Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
Disulfide bondi521 ↔ 533PROSITE-ProRule annotation
Disulfide bondi539 ↔ 549PROSITE-ProRule annotation
Disulfide bondi544 ↔ 558PROSITE-ProRule annotation
Disulfide bondi560 ↔ 573PROSITE-ProRule annotation
Disulfide bondi579 ↔ 591PROSITE-ProRule annotation
Disulfide bondi586 ↔ 600PROSITE-ProRule annotation
Disulfide bondi602 ↔ 615PROSITE-ProRule annotation
Disulfide bondi621 ↔ 632PROSITE-ProRule annotation
Disulfide bondi627 ↔ 641PROSITE-ProRule annotation
Disulfide bondi643 ↔ 656PROSITE-ProRule annotation
Disulfide bondi662 ↔ 673PROSITE-ProRule annotation
Disulfide bondi668 ↔ 682PROSITE-ProRule annotation
Disulfide bondi684 ↔ 697PROSITE-ProRule annotation
Disulfide bondi772 ↔ 784PROSITE-ProRule annotation
Disulfide bondi779 ↔ 793PROSITE-ProRule annotation
Disulfide bondi795 ↔ 808PROSITE-ProRule annotation
Disulfide bondi814 ↔ 826PROSITE-ProRule annotation
Disulfide bondi821 ↔ 835PROSITE-ProRule annotation
Disulfide bondi837 ↔ 850PROSITE-ProRule annotation
Disulfide bondi856 ↔ 866PROSITE-ProRule annotation
Disulfide bondi861 ↔ 875PROSITE-ProRule annotation
Disulfide bondi877 ↔ 890PROSITE-ProRule annotation
Disulfide bondi959 ↔ 971PROSITE-ProRule annotation
Disulfide bondi966 ↔ 980PROSITE-ProRule annotation
Disulfide bondi982 ↔ 995PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1089PROSITE-ProRule annotation
Disulfide bondi1084 ↔ 1098PROSITE-ProRule annotation
Disulfide bondi1100 ↔ 1113PROSITE-ProRule annotation
Glycosylationi1112N-linked (GlcNAc...)1 Publication1
Disulfide bondi1119 ↔ 1131PROSITE-ProRule annotation
Disulfide bondi1126 ↔ 1140PROSITE-ProRule annotation
Disulfide bondi1142 ↔ 1156PROSITE-ProRule annotation
Disulfide bondi1162 ↔ 1174PROSITE-ProRule annotation
Disulfide bondi1169 ↔ 1183PROSITE-ProRule annotation
Disulfide bondi1185 ↔ 1198PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1216PROSITE-ProRule annotation
Disulfide bondi1211 ↔ 1225PROSITE-ProRule annotation
Disulfide bondi1227 ↔ 1240PROSITE-ProRule annotation
Disulfide bondi1246 ↔ 1257PROSITE-ProRule annotation
Disulfide bondi1253 ↔ 1266PROSITE-ProRule annotation
Disulfide bondi1268 ↔ 1281PROSITE-ProRule annotation
Disulfide bondi1287 ↔ 1299PROSITE-ProRule annotation
Disulfide bondi1294 ↔ 1308PROSITE-ProRule annotation
Disulfide bondi1310 ↔ 1323PROSITE-ProRule annotation
Disulfide bondi1329 ↔ 1341PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1350PROSITE-ProRule annotation
Disulfide bondi1352 ↔ 1365PROSITE-ProRule annotation
Disulfide bondi1371 ↔ 1384PROSITE-ProRule annotation
Disulfide bondi1378 ↔ 1393PROSITE-ProRule annotation
Disulfide bondi1395 ↔ 1406PROSITE-ProRule annotation
Disulfide bondi1412 ↔ 1425PROSITE-ProRule annotation
Glycosylationi1414N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1419 ↔ 1434PROSITE-ProRule annotation
Disulfide bondi1436 ↔ 1447PROSITE-ProRule annotation
Disulfide bondi1453 ↔ 1465PROSITE-ProRule annotation
Disulfide bondi1460 ↔ 1474PROSITE-ProRule annotation
Disulfide bondi1476 ↔ 1489PROSITE-ProRule annotation
Disulfide bondi1495 ↔ 1506PROSITE-ProRule annotation
Disulfide bondi1501 ↔ 1515PROSITE-ProRule annotation
Disulfide bondi1517 ↔ 1530PROSITE-ProRule annotation
Glycosylationi1529N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1536 ↔ 1547PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1556PROSITE-ProRule annotation
Disulfide bondi1558 ↔ 1571PROSITE-ProRule annotation
Glycosylationi1625N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1654 ↔ 1666PROSITE-ProRule annotation
Disulfide bondi1661 ↔ 1675PROSITE-ProRule annotation
Disulfide bondi1677 ↔ 1690PROSITE-ProRule annotation
Disulfide bondi1696 ↔ 1708PROSITE-ProRule annotation
Disulfide bondi1703 ↔ 1717PROSITE-ProRule annotation
Glycosylationi1714N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1719 ↔ 1732PROSITE-ProRule annotation
Glycosylationi1745N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1756N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1812 ↔ 1824PROSITE-ProRule annotation
Disulfide bondi1819 ↔ 1833PROSITE-ProRule annotation
Disulfide bondi1835 ↔ 1848PROSITE-ProRule annotation
Disulfide bondi1854 ↔ 1867PROSITE-ProRule annotation
Disulfide bondi1861 ↔ 1876PROSITE-ProRule annotation
Disulfide bondi1878 ↔ 1890PROSITE-ProRule annotation
Disulfide bondi1896 ↔ 1908PROSITE-ProRule annotation
Disulfide bondi1903 ↔ 1917PROSITE-ProRule annotation
Disulfide bondi1919 ↔ 1932PROSITE-ProRule annotation
Disulfide bondi1938 ↔ 1948PROSITE-ProRule annotation
Disulfide bondi1943 ↔ 1957PROSITE-ProRule annotation
Glycosylationi1945N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1959 ↔ 1971PROSITE-ProRule annotation
Disulfide bondi1977 ↔ 1990PROSITE-ProRule annotation
Disulfide bondi1985 ↔ 1999PROSITE-ProRule annotation
Disulfide bondi2001 ↔ 2014PROSITE-ProRule annotation
Disulfide bondi2020 ↔ 2032PROSITE-ProRule annotation
Disulfide bondi2027 ↔ 2041PROSITE-ProRule annotation
Disulfide bondi2043 ↔ 2054PROSITE-ProRule annotation
Disulfide bondi2060 ↔ 2072PROSITE-ProRule annotation
Disulfide bondi2067 ↔ 2081PROSITE-ProRule annotation
Disulfide bondi2083 ↔ 2096PROSITE-ProRule annotation
Glycosylationi2120N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2175 ↔ 2187PROSITE-ProRule annotation
Disulfide bondi2182 ↔ 2196PROSITE-ProRule annotation
Disulfide bondi2198 ↔ 2211PROSITE-ProRule annotation
Disulfide bondi2217 ↔ 2228PROSITE-ProRule annotation
Disulfide bondi2223 ↔ 2237PROSITE-ProRule annotation
Glycosylationi2225N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2239 ↔ 2251PROSITE-ProRule annotation
Disulfide bondi2257 ↔ 2268PROSITE-ProRule annotation
Disulfide bondi2264 ↔ 2277PROSITE-ProRule annotation
Disulfide bondi2279 ↔ 2292PROSITE-ProRule annotation
Disulfide bondi2298 ↔ 2312PROSITE-ProRule annotation
Disulfide bondi2305 ↔ 2321PROSITE-ProRule annotation
Disulfide bondi2323 ↔ 2336PROSITE-ProRule annotation
Disulfide bondi2342 ↔ 2354PROSITE-ProRule annotation
Disulfide bondi2349 ↔ 2363PROSITE-ProRule annotation
Disulfide bondi2365 ↔ 2378PROSITE-ProRule annotation
Disulfide bondi2453 ↔ 2465PROSITE-ProRule annotation
Disulfide bondi2460 ↔ 2474PROSITE-ProRule annotation
Disulfide bondi2476 ↔ 2489PROSITE-ProRule annotation
Disulfide bondi2495 ↔ 2506PROSITE-ProRule annotation
Disulfide bondi2502 ↔ 2515PROSITE-ProRule annotation
Disulfide bondi2517 ↔ 2530PROSITE-ProRule annotation
Disulfide bondi2536 ↔ 2547PROSITE-ProRule annotation
Disulfide bondi2543 ↔ 2556PROSITE-ProRule annotation
Disulfide bondi2558 ↔ 2569PROSITE-ProRule annotation
Disulfide bondi2575 ↔ 2588PROSITE-ProRule annotation
Disulfide bondi2582 ↔ 2597PROSITE-ProRule annotation
Disulfide bondi2599 ↔ 2612PROSITE-ProRule annotation
Disulfide bondi2618 ↔ 2628PROSITE-ProRule annotation
Disulfide bondi2624 ↔ 2637PROSITE-ProRule annotation
Disulfide bondi2639 ↔ 2652PROSITE-ProRule annotation
Disulfide bondi2658 ↔ 2669PROSITE-ProRule annotation
Disulfide bondi2664 ↔ 2678PROSITE-ProRule annotation
Disulfide bondi2680 ↔ 2693PROSITE-ProRule annotation
Disulfide bondi2699 ↔ 2710PROSITE-ProRule annotation
Disulfide bondi2706 ↔ 2719PROSITE-ProRule annotation
Disulfide bondi2721 ↔ 2733PROSITE-ProRule annotation
Glycosylationi2808N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP35556.
MaxQBiP35556.
PaxDbiP35556.
PeptideAtlasiP35556.
PRIDEiP35556.

PTM databases

iPTMnetiP35556.
PhosphoSitePlusiP35556.

Expressioni

Tissue specificityi

Expressed in fetal eye (18 weeks)in the retinal pigment epithelium (RPE), the choroid, Bruch's membrane and in the sclera. Not expressed in the neural retina.1 Publication

Gene expression databases

BgeeiENSG00000138829.
CleanExiHS_FBN2.
ExpressionAtlasiP35556. baseline and differential.
GenevisibleiP35556. HS.

Organism-specific databases

HPAiCAB026401.
HPA012853.

Interactioni

Subunit structurei

Interacts with BMP2, BMP4, BMP7, BMP10 and GDF5 (PubMed:18339631). Interacts with MFAP2 and MFAP5 (PubMed:15131124). Interacts with ADAMTSL5 (PubMed:23010571). Interacts with MFAP4 (PubMed:26601954).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FBN1P355552EBI-6164392,EBI-2505934
FN1P027512EBI-6164392,EBI-1220319

Protein-protein interaction databases

BioGridi108495. 17 interactors.
IntActiP35556. 7 interactors.
STRINGi9606.ENSP00000262464.

Structurei

3D structure databases

ProteinModelPortaliP35556.
SMRiP35556.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini111 – 142EGF-like 1PROSITE-ProRule annotationAdd BLAST32
Domaini145 – 176EGF-like 2PROSITE-ProRule annotationAdd BLAST32
Domaini176 – 208EGF-like 3PROSITE-ProRule annotationAdd BLAST33
Domaini214 – 266TB 1Add BLAST53
Domaini276 – 317EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini318 – 359EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini364 – 417TB 2Add BLAST54
Domaini494 – 534EGF-like 6PROSITE-ProRule annotationAdd BLAST41
Domaini535 – 574EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini575 – 616EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini617 – 657EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini658 – 698EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini704 – 756TB 3Add BLAST53
Domaini768 – 809EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini810 – 851EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini852 – 891EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini896 – 947TB 4Add BLAST52
Domaini955 – 996EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1001 – 1052TB 5Add BLAST52
Domaini1073 – 1114EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1115 – 1157EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1158 – 1199EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1200 – 1241EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1242 – 1282EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1283 – 1324EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1325 – 1366EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1367 – 1407EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1408 – 1448EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1449 – 1490EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1491 – 1531EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1532 – 1572EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1577 – 1633TB 6Add BLAST57
Domaini1650 – 1691EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1692 – 1733EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1738 – 1791TB 7Add BLAST54
Domaini1808 – 1849EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1850 – 1891EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1892 – 1933EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1934 – 1972EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini1973 – 2015EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini2016 – 2055EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2056 – 2097EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2102 – 2155TB 8Add BLAST54
Domaini2171 – 2212EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2213 – 2252EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2253 – 2293EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2294 – 2337EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini2338 – 2379EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2384 – 2437TB 9Add BLAST54
Domaini2449 – 2490EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini2491 – 2531EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2532 – 2570EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2571 – 2613EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini2614 – 2653EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini2654 – 2694EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini2695 – 2734EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni149 – 359Interaction with MFAP41 PublicationAdd BLAST211
Regioni1735 – 2171Interaction with MFAP41 PublicationAdd BLAST437

Sequence similaritiesi

Belongs to the fibrillin family.Curated
Contains 47 EGF-like domains.PROSITE-ProRule annotation
Contains 9 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP35556.
OMAiAEFHGLC.
OrthoDBiEOG091G002H.
PhylomeDBiP35556.
TreeFamiTF316849.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF12661. hEGF. 2 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 46 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35556-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA
60 70 80 90 100
TAGSEGGFLA PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG
110 120 130 140 150
WKTLPGGNQC IVPICRNSCG DGFCSRPNMC TCSSGQISST CGSKSIQQCS
160 170 180 190 200
VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC ENGCQNGGRC IGPNRCACVY
210 220 230 240 250
GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC ATIGRAWGHP
260 270 280 290 300
CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE
310 320 330 340 350
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV
360 370 380 390 400
TSTDGSRCID QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT
410 420 430 440 450
IPEACPVRGS EEYRRLCMDG LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG
460 470 480 490 500
YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG QGPIITGLTI LNQTIDICKH
510 520 530 540 550
HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT SNPCTNGDCV
560 570 580 590 600
NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC
610 620 630 640 650
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA
660 670 680 690 700
PNGRYCTDVD ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT
710 720 730 740 750
HMRSTCYGGI KKGVCVRPFP GAVTKSECCC ANPDYGFGEP CQPCPAKNSA
760 770 780 790 800
EFHGLCSSGV GITVDGRDIN ECALDPDICA NGICENLRGS YRCNCNSGYE
810 820 830 840 850
PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG YVFRTETETC
860 870 880 890 900
EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL
910 920 930 940 950
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG
960 970 980 990 1000
VTCEDVNECE VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM
1010 1020 1030 1040 1050
EQCYLKWDED ECIHPVPGKF RMDACCCAVG AAWGTECEEC PKPGTKEYET
1060 1070 1080 1090 1100
LCPRGAGFAN RGDVLTGRPF YKDINECKAF PGMCTYGKCR NTIGSFKCRC
1110 1120 1130 1140 1150
NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC ECFEGYESGF
1160 1170 1180 1190 1200
MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD
1210 1220 1230 1240 1250
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN
1260 1270 1280 1290 1300
GGCDTQCTNS EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT
1310 1320 1330 1340 1350
NIPGEYRCLC YDGFMASMDM KTCIDVNECD LNSNICMFGE CENTKGSFIC
1360 1370 1380 1390 1400
HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM HASCLNIPGS FKCSCREGWI
1410 1420 1430 1440 1450
GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF TGDGFTCSDV
1460 1470 1480 1490 1500
DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI
1510 1520 1530 1540 1550
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT
1560 1570 1580 1590 1600
PGRYECNCPP DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG
1610 1620 1630 1640 1650
VSRSSCCCSL GKAWGNPCET CPPVNSTEYY TLCPGGEGFR PNPITIILED
1660 1670 1680 1690 1700
IDECQELPGL CQGGNCINTF GSFQCECPQG YYLSEDTRIC EDIDECFAHP
1710 1720 1730 1740 1750
GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC YRSYNGTTCE
1760 1770 1780 1790 1800
NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD
1810 1820 1830 1840 1850
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED
1860 1870 1880 1890 1900
IDECSNGDNL CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP
1910 1920 1930 1940 1950
NVCSHGLCVD LQGSYQCICH NGFKASQDQT MCMDVDECER HPCGNGTCKN
1960 1970 1980 1990 2000
TVGSYNCLCY PGFELTHNND CLDIDECSSF FGQVCRNGRC FNEIGSFKCL
2010 2020 2030 2040 2050
CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR CICPPGYEVK
2060 2070 2080 2090 2100
SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR
2110 2120 2130 2140 2150
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA
2160 2170 2180 2190 2200
FQDLCPYGHG TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM
2210 2220 2230 2240 2250
GYNLDYTGVR CVDTDECSIG NPCGNGTCTN VIGSFECNCN EGFEPGPMMN
2260 2270 2280 2290 2300
CEDINECAQN PLLCAFRCMN TFGSYECTCP IGYALREDQK MCKDLDECAE
2310 2320 2330 2340 2350
GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN ECRTKPGICE
2360 2370 2380 2390 2400
NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS
2410 2420 2430 2440 2450
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI
2460 2470 2480 2490 2500
DECKVMPNLC TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK
2510 2520 2530 2540 2550
PCNYICKNTE GSYQCSCPRG YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT
2560 2570 2580 2590 2600
LGGFTCKCPP GFTQHHTACI DNNECGSQPS LCGAKGICQN TPGSFSCECQ
2610 2620 2630 2640 2650
RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP QGYIQHYQWN
2660 2670 2680 2690 2700
QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS
2710 2720 2730 2740 2750
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE
2760 2770 2780 2790 2800
VDEENALSPE ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD
2810 2820 2830 2840 2850
SPVNMKFNLS HLGSKEHILE LRPAIQPLNN HIRYVISQGN DDSVFRIHQR
2860 2870 2880 2890 2900
NGLSYLHTAK KKLMPGTYTL EITSIPLYKK KELKKLEESN EDDYLLGELG
2910
EALRMRLQIQ LY
Length:2,912
Mass (Da):314,775
Last modified:May 26, 2009 - v3
Checksum:i0F0D78319E9911E6
GO
Isoform 2 (identifier: P35556-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-145: Missing.
     1491-1506: DIDECSFQNICVFGTC → GGSPGFQLIFKLDQPQ
     1507-2912: Missing.

Show »
Length:1,473
Mass (Da):157,690
Checksum:i2B6620CFCA6F7A72
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti146I → L in BAG62163 (PubMed:14702039).Curated1
Sequence conflicti192 – 195GPNR → AQP in AAA18950 (PubMed:8120105).Curated4
Sequence conflicti243I → T in AAA18950 (PubMed:8120105).Curated1
Sequence conflicti243I → T in BAG62163 (PubMed:14702039).Curated1
Sequence conflicti1161E → G in AAA18950 (PubMed:8120105).Curated1
Sequence conflicti1161E → G in CAB56757 (PubMed:1852206).Curated1
Sequence conflicti1244D → G in BAG62163 (PubMed:14702039).Curated1
Sequence conflicti1409L → R in CAB56757 (PubMed:1852206).Curated1
Sequence conflicti1503F → S in AAA18950 (PubMed:8120105).Curated1
Sequence conflicti2584A → G in AAA18950 (PubMed:8120105).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015851391E → K in DA9. Corresponds to variant rs137852826dbSNPEnsembl.1
Natural variantiVAR_054979594T → S.2 Publications1
Natural variantiVAR_054980681R → H.1 PublicationCorresponds to variant rs548605398dbSNPEnsembl.1
Natural variantiVAR_058364754G → S in DA9. 1 PublicationCorresponds to variant rs145259927dbSNPEnsembl.1
Natural variantiVAR_002349965V → I.4 PublicationsCorresponds to variant rs154001dbSNPEnsembl.1
Natural variantiVAR_0549811057G → D in DA9. 2 Publications1
Natural variantiVAR_0583651091N → S in DA9. 1 Publication1
Natural variantiVAR_0549821093I → T in DA9. 2 Publications1
Natural variantiVAR_0107391115D → H in DA9; the underlying nucleotide substitution also causes low level in-frame mis-splicing of exon 25. 2 PublicationsCorresponds to variant rs137852827dbSNPEnsembl.1
Natural variantiVAR_0583661122S → P in DA9. 1 Publication1
Natural variantiVAR_0107401142C → F in DA9. 2 PublicationsCorresponds to variant rs137852828dbSNPEnsembl.1
Natural variantiVAR_0583671142C → R in DA9. 1 Publication1
Natural variantiVAR_0726511144E → K in EOMD. 1 PublicationCorresponds to variant rs200060005dbSNPEnsembl.1
Natural variantiVAR_0583681146Y → C in DA9. 1 Publication1
Natural variantiVAR_0583691156C → F in DA9. 1 Publication1
Natural variantiVAR_0583701161E → K in DA9. 1 Publication1
Natural variantiVAR_0549831179G → C in DA9. 1 Publication1
Natural variantiVAR_0549841198C → Y in DA9. 1 Publication1
Natural variantiVAR_0549851240C → R in DA9. 1 Publication1
Natural variantiVAR_0583711246C → F in DA9. 1 Publication1
Natural variantiVAR_0726521247M → T in EOMD. 1 PublicationCorresponds to variant rs149054177dbSNPEnsembl.1
Natural variantiVAR_0107411253C → W in DA9. 2 PublicationsCorresponds to variant rs28931602dbSNPEnsembl.1
Natural variantiVAR_0023501253C → Y in DA9. 2 PublicationsCorresponds to variant rs137852825dbSNPEnsembl.1
Natural variantiVAR_0764821257C → R in DA9. 1 Publication1
Natural variantiVAR_0549861257C → W in DA9. 1 Publication1
Natural variantiVAR_0726531259N → K in DA9. 1 PublicationCorresponds to variant rs267606802dbSNPEnsembl.1
Natural variantiVAR_0549871268C → R in DA9. 1 Publication1
Natural variantiVAR_0726541381H → N.1 PublicationCorresponds to variant rs78727187dbSNPEnsembl.1
Natural variantiVAR_0583721384C → F in DA9. 1 Publication1
Natural variantiVAR_0583731384C → Y in DA9. 1 PublicationCorresponds to variant rs794727560dbSNPEnsembl.1
Natural variantiVAR_0740521406C → R in DA9. 1 Publication1
Natural variantiVAR_0583741408D → N in DA9. 1 Publication1
Natural variantiVAR_0726551416T → A.1 PublicationCorresponds to variant rs200837433dbSNPEnsembl.1
Natural variantiVAR_0583751425C → R in DA9. 1 Publication1
Natural variantiVAR_0023511434C → S in DA9. 2 Publications1
Natural variantiVAR_0726561438E → K.1 PublicationCorresponds to variant rs56168072dbSNPEnsembl.1
Natural variantiVAR_0549881772W → G.2 Publications1
Natural variantiVAR_0647052062E → V Found in a renal cell carcinoma case; somatic mutation. 1 Publication1
Natural variantiVAR_0549892266F → L.2 Publications1
Natural variantiVAR_0554152278T → M.Corresponds to variant rs2307109dbSNPEnsembl.1
Natural variantiVAR_0554162311M → V.Corresponds to variant rs32209dbSNPEnsembl.1
Natural variantiVAR_0161432428P → T.1 PublicationCorresponds to variant rs1801169dbSNPEnsembl.1
Natural variantiVAR_0554172580S → L.1 PublicationCorresponds to variant rs2291628dbSNPEnsembl.1
Natural variantiVAR_0549902581L → S.Corresponds to variant rs2291628dbSNPEnsembl.1
Natural variantiVAR_0146642771S → P.2 PublicationsCorresponds to variant rs1801170dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_037369113 – 145Missing in isoform 2. 2 PublicationsAdd BLAST33
Alternative sequenceiVSP_0373701491 – 1506DIDEC…VFGTC → GGSPGFQLIFKLDQPQ in isoform 2. 2 PublicationsAdd BLAST16
Alternative sequenceiVSP_0373711507 – 2912Missing in isoform 2. 2 PublicationsAdd BLAST1406

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03272 mRNA. Translation: AAA18950.1.
AK300440 mRNA. Translation: BAG62163.1.
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1.
AB209735 mRNA. Translation: BAD92972.1.
CCDSiCCDS34222.1. [P35556-1]
PIRiA54105.
RefSeqiNP_001990.2. NM_001999.3. [P35556-1]
UniGeneiHs.519294.

Genome annotation databases

EnsembliENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
GeneIDi2201.
KEGGihsa:2201.
UCSCiuc003kuu.3. human. [P35556-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03272 mRNA. Translation: AAA18950.1.
AK300440 mRNA. Translation: BAG62163.1.
AC025169 Genomic DNA. No translation available.
AC034235 Genomic DNA. No translation available.
AC113387 Genomic DNA. No translation available.
X62009 mRNA. Translation: CAB56757.1.
AB209735 mRNA. Translation: BAD92972.1.
CCDSiCCDS34222.1. [P35556-1]
PIRiA54105.
RefSeqiNP_001990.2. NM_001999.3. [P35556-1]
UniGeneiHs.519294.

3D structure databases

ProteinModelPortaliP35556.
SMRiP35556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108495. 17 interactors.
IntActiP35556. 7 interactors.
STRINGi9606.ENSP00000262464.

PTM databases

iPTMnetiP35556.
PhosphoSitePlusiP35556.

Polymorphism and mutation databases

BioMutaiFBN2.
DMDMi238054385.

Proteomic databases

EPDiP35556.
MaxQBiP35556.
PaxDbiP35556.
PeptideAtlasiP35556.
PRIDEiP35556.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262464; ENSP00000262464; ENSG00000138829. [P35556-1]
ENST00000508053; ENSP00000424571; ENSG00000138829. [P35556-1]
GeneIDi2201.
KEGGihsa:2201.
UCSCiuc003kuu.3. human. [P35556-1]

Organism-specific databases

CTDi2201.
DisGeNETi2201.
GeneCardsiFBN2.
GeneReviewsiFBN2.
H-InvDBHIX0005141.
HIX0137461.
HGNCiHGNC:3604. FBN2.
HPAiCAB026401.
HPA012853.
MalaCardsiFBN2.
MIMi121050. phenotype.
612570. gene.
616118. phenotype.
neXtProtiNX_P35556.
OpenTargetsiENSG00000138829.
Orphaneti279. Age-related macular degeneration.
115. Congenital contractural arachnodactyly.
PharmGKBiPA28017.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiP35556.
OMAiAEFHGLC.
OrthoDBiEOG091G002H.
PhylomeDBiP35556.
TreeFamiTF316849.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138829-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1566948. Elastic fibre formation.
R-HSA-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiFBN2. human.
GenomeRNAii2201.
PROiP35556.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138829.
CleanExiHS_FBN2.
ExpressionAtlasiP35556. baseline and differential.
GenevisibleiP35556. HS.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF12661. hEGF. 2 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 46 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFBN2_HUMAN
AccessioniPrimary (citable) accession number: P35556
Secondary accession number(s): B4DU01, Q59ES6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: May 26, 2009
Last modified: November 30, 2016
This is version 180 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.